Multiple Interactions of the Intrinsically Disordered Region between the Helicase and Nuclease Domains of the Archaeal Hef Protein
Year: 2014
Type: article
Abstract: Hef is an archaeal protein that probably functions mainly in stalled replication fork repair. The presence of an unstructured region was predicted between the two distinct domains of the Hef protein. We analyzed the interdomain region of Thermococcus kodakarensis Hef and demonstrated its disordered structure by CD, NMR, and high speed atomic force microscopy (AFM). To investigate the functions of this intrinsically disordered region (IDR), we screened for proteins interacting with the IDR of Hef by a yeast two-hybrid method, and 10 candidate proteins were obtained. We found that PCNA1 and a RecJ-like protein specifically bind to the IDR in vitro. These results suggested that the Hef protein interacts with several different proteins that work together in the pathways downstream from stalled replication fork repair by converting the IDR structure depending on the partner protein.
Source: Journal of Biological Chemistry
Institutions: Kyushu University, Kanazawa University, Nagoya University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
Awards: Studies on genome integrity of archaea in the extremophilic environments, Study on the motile mechanisms for processive myosins with short legs using high-speed atomic force microscopy, Opening up New Structural Biology by High-speed AFM, Medicinal application of intrinsically disordered proteins of unknown function
OpenAlex ID: W2094880366